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Structural insights into urokinase-type plasminogen activator receptor (uPAR) dimerization reveal significant conformational changes. A specific mutation (E49P) promotes dimer formation, impacting receptor binding and cellular functions.

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Cell Biology

Background:

  • Receptor dimerization of urokinase-type plasminogen activator receptor (uPAR) is known at the protein and cell surface levels.
  • A dimeric form of mouse uPAR isoform 2 has been implicated in kidney disease.

Purpose of the Study:

  • To determine the crystal structure of the human uPAR dimer.
  • To elucidate the structural basis of uPAR dimerization and its functional consequences.

Main Methods:

  • X-ray crystallography at 2.96 Å resolution.
  • Identification and characterization of a mutation (E49P) promoting uPAR dimerization.

Main Results:

  • The crystal structure reveals significant conformational changes in the dimeric uPAR, with domain D1 opening to form an expanded ring and β-sheet, creating an intertwined dimer.
  • The E49P mutation was identified as promoting dimer formation.
  • Dimerization enhances uPAR binding to the amino terminal fragment of uPA, promotes basal membrane localization, stimulates cell proliferation, and alters cell morphology through β1 integrin signaling.

Conclusions:

  • The study provides the first crystal structure of a human uPAR dimer, revealing its unique quaternary structure.
  • The findings elucidate the structural mechanisms underlying uPAR dimerization and its impact on cellular processes.
  • This work lays the foundation for further investigation into the multifaceted roles of uPAR.